Kim Y W, Wang H, Sures I, Lammers R, Martell K J, Ullrich A
Department of Molecular Biology, Max-Planck-Institut für Biochemie, Martinsried, Germany.
Oncogene. 1996 Nov 21;13(10):2275-9.
Using a polymerase chain reaction (PCR) amplification strategy, we identified a novel protein tyrosine phosphatase (PTPase) designated Brain Derived Phosphatase (BDP1). The full length sequence encoded an open reading frame of 459 amino acids with no transmembrane domain and had a calculated molecular weight of 50 kDa. The predicted amino acid sequence contained a PEST motif and accordingly, BDP1 shared the greatest homology with members of the PTP-PEST family. When transiently expressed in 293 cells BDP1 hydrolyzed p-Nitrophenylphosphate, confirming it as a functional protein tyrosine phosphatase. Northern blot analysis indicated that BDP1 was expressed not only in brain, but also in colon and several different tumor-derived cell lines. Furthermore, BDP1 was found to differentially dephosphorylate autophosphorylated tyrosine kinases which are known to be overexpressed in tumor tissues.
通过聚合酶链反应（PCR）扩增策略，我们鉴定出一种新型蛋白质酪氨酸磷酸酶（PTPase），命名为脑源性磷酸酶（BDP1）。全长序列编码一个459个氨基酸的开放阅读框，无跨膜结构域，计算分子量为50 kDa。预测的氨基酸序列包含一个PEST基序，因此，BDP1与PTP-PEST家族成员具有最大的同源性。当在293细胞中瞬时表达时，BDP1可水解对硝基苯磷酸酯，证实其为一种功能性蛋白质酪氨酸磷酸酶。Northern印迹分析表明，BDP1不仅在脑中表达，在结肠和几种不同的肿瘤来源细胞系中也有表达。此外，发现BDP1对已知在肿瘤组织中过表达的自磷酸化酪氨酸激酶进行差异性去磷酸化。
